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Q9UK32

- KS6A6_HUMAN

UniProt

Q9UK32 - KS6A6_HUMAN

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Protein

Ribosomal protein S6 kinase alpha-6

Gene

RPS6KA6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Constitutively active serine/threonine-protein kinase that exhibits growth-factor-independent kinase activity and that may participate in p53/TP53-dependent cell growth arrest signaling and play an inhibitory role during embryogenesis.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.By similarity

Enzyme regulationi

Constitutively activated by phosphorylation at Ser-232, Ser-372, and Ser-389 in serum-starved cells. Does not require growth factor stimulation for significant kinase activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051ATPPROSITE-ProRule annotation
Active sitei198 – 1981Proton acceptorBy similarity
Binding sitei455 – 4551ATPPROSITE-ProRule annotation
Active sitei543 – 5431Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi79 – 879ATPPROSITE-ProRule annotation
Nucleotide bindingi432 – 4409ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. protein kinase activity Source: ProtInc
  4. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. axon guidance Source: Reactome
  2. central nervous system development Source: ProtInc
  3. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: UniProtKB
  4. negative regulation of embryonic development Source: UniProtKB
  5. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  6. negative regulation of mesoderm development Source: UniProtKB
  7. signal transduction Source: ProtInc
  8. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_20510. RSK activation.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_22365. Recycling pathway of L1.
SignaLinkiQ9UK32.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase alpha-6 (EC:2.7.11.1)
Short name:
S6K-alpha-6
Alternative name(s):
90 kDa ribosomal protein S6 kinase 6
Short name:
p90-RSK 6
Short name:
p90RSK6
Ribosomal S6 kinase 4
Short name:
RSK-4
pp90RSK4
Gene namesi
Name:RPS6KA6
Synonyms:RSK4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:10435. RPS6KA6.

Subcellular locationi

Cytoplasmcytosol 1 Publication. Nucleus 1 Publication
Note: Predominantly cytosolic.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi372 – 3721S → A: No effect on activity. 1 Publication
Mutagenesisi389 – 3891S → A: Strongly decreases activity. 1 Publication
Mutagenesisi581 – 5811T → A: No effect on activity. 1 Publication

Organism-specific databases

PharmGKBiPA34850.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 745745Ribosomal protein S6 kinase alpha-6PRO_0000086209Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei232 – 2321Phosphoserine1 Publication
Modified residuei372 – 3721Phosphoserine1 Publication
Modified residuei389 – 3891Phosphoserine2 Publications
Modified residuei581 – 5811Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated at Ser-232, Ser-372, and Ser-389 in serum-starved cells.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UK32.
PaxDbiQ9UK32.
PRIDEiQ9UK32.

PTM databases

PhosphoSiteiQ9UK32.

Expressioni

Gene expression databases

BgeeiQ9UK32.
CleanExiHS_RPS6KA6.
ExpressionAtlasiQ9UK32. baseline and differential.
GenevestigatoriQ9UK32.

Organism-specific databases

HPAiHPA002852.
HPA003904.

Interactioni

Subunit structurei

Forms a complex with MAPK3/ERK1 but not with MAPK9 or MAPK14 in serum-starved cells.

Protein-protein interaction databases

BioGridi118144. 38 interactions.
IntActiQ9UK32. 28 interactions.
MINTiMINT-1424416.
STRINGi9606.ENSP00000262752.

Structurei

3D structure databases

ProteinModelPortaliQ9UK32.
SMRiQ9UK32. Positions 21-714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 330258Protein kinase 1PROSITE-ProRule annotationAdd
BLAST
Domaini331 – 40070AGC-kinase C-terminalAdd
BLAST
Domaini426 – 683258Protein kinase 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 2 protein kinase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119016.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ9UK32.
KOiK04373.
OrthoDBiEOG7B8S38.
PhylomeDBiQ9UK32.
TreeFamiTF313438.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016239. Ribosomal_S6_kinase_II.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UK32) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLPFAPQDEP WDREMEVFSG GGASSGEVNG LKMVDEPMEE GEADSCHDEG
60 70 80 90 100
VVKEIPITHH VKEGYEKADP AQFELLKVLG QGSFGKVFLV RKKTGPDAGQ
110 120 130 140 150
LYAMKVLKKA SLKVRDRVRT KMERDILVEV NHPFIVKLHY AFQTEGKLYL
160 170 180 190 200
ILDFLRGGDV FTRLSKEVLF TEEDVKFYLA ELALALDHLH QLGIVYRDLK
210 220 230 240 250
PENILLDEIG HIKLTDFGLS KESVDQEKKA YSFCGTVEYM APEVVNRRGH
260 270 280 290 300
SQSADWWSYG VLMFEMLTGT LPFQGKDRNE TMNMILKAKL GMPQFLSAEA
310 320 330 340 350
QSLLRMLFKR NPANRLGSEG VEEIKRHLFF ANIDWDKLYK REVQPPFKPA
360 370 380 390 400
SGKPDDTFCF DPEFTAKTPK DSPGLPASAN AHQLFKGFSF VATSIAEEYK
410 420 430 440 450
ITPITSANVL PIVQINGNAA QFGEVYELKE DIGVGSYSVC KRCIHATTNM
460 470 480 490 500
EFAVKIIDKS KRDPSEEIEI LMRYGQHPNI ITLKDVFDDG RYVYLVTDLM
510 520 530 540 550
KGGELLDRIL KQKCFSEREA SDILYVISKT VDYLHCQGVV HRDLKPSNIL
560 570 580 590 600
YMDESASADS IRICDFGFAK QLRGENGLLL TPCYTANFVA PEVLMQQGYD
610 620 630 640 650
AACDIWSLGV LFYTMLAGYT PFANGPNDTP EEILLRIGNG KFSLSGGNWD
660 670 680 690 700
NISDGAKDLL SHMLHMDPHQ RYTAEQILKH SWITHRDQLP NDQPKRNDVS
710 720 730 740
HVVKGAMVAT YSALTHKTFQ PVLEPVAASS LAQRRSMKKR TSTGL
Length:745
Mass (Da):83,872
Last modified:May 1, 2000 - v1
Checksum:i5EC5AB2FA1C19DE8
GO
Isoform 2 (identifier: Q9UK32-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: MLPFAPQDEPWDREMEVFSGGGASSGE → MGLSTSAIWKNTRVEIVNPYEVKRKVK

Note: No experimental confirmation available.

Show »
Length:745
Mass (Da):84,093
Checksum:iD8EB15DB8C280DDD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161D → G in CAG38803. 1 PublicationCurated
Sequence conflicti295 – 2951F → L in CAG38803. 1 PublicationCurated
Sequence conflicti341 – 3411R → G in CAG38803. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401Y → C in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_040637
Natural varianti258 – 2581S → T in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040638
Natural varianti692 – 6921D → N.1 Publication
Corresponds to variant rs6616890 [ dbSNP | Ensembl ].
VAR_030670

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2727MLPFA…ASSGE → MGLSTSAIWKNTRVEIVNPY EVKRKVK in isoform 2. 1 PublicationVSP_056181Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF184965 mRNA. Translation: AAF13190.1.
CR536566 mRNA. Translation: CAG38803.1.
AK313240 mRNA. Translation: BAG36051.1.
AL389887, AL354653 Genomic DNA. Translation: CAC16111.2.
AL354653, AL389887 Genomic DNA. Translation: CAD13486.2.
CH471104 Genomic DNA. Translation: EAW98575.1.
BC143648 mRNA. Translation: AAI43649.1.
CCDSiCCDS14451.1. [Q9UK32-1]
RefSeqiNP_055311.1. NM_014496.4.
UniGeneiHs.234478.

Genome annotation databases

EnsembliENST00000262752; ENSP00000262752; ENSG00000072133. [Q9UK32-1]
ENST00000543399; ENSP00000440830; ENSG00000072133. [Q9UK32-2]
ENST00000620340; ENSP00000483896; ENSG00000072133. [Q9UK32-2]
GeneIDi27330.
KEGGihsa:27330.
UCSCiuc004eej.2. human. [Q9UK32-1]

Polymorphism databases

DMDMi11133131.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF184965 mRNA. Translation: AAF13190.1 .
CR536566 mRNA. Translation: CAG38803.1 .
AK313240 mRNA. Translation: BAG36051.1 .
AL389887 , AL354653 Genomic DNA. Translation: CAC16111.2 .
AL354653 , AL389887 Genomic DNA. Translation: CAD13486.2 .
CH471104 Genomic DNA. Translation: EAW98575.1 .
BC143648 mRNA. Translation: AAI43649.1 .
CCDSi CCDS14451.1. [Q9UK32-1 ]
RefSeqi NP_055311.1. NM_014496.4.
UniGenei Hs.234478.

3D structure databases

ProteinModelPortali Q9UK32.
SMRi Q9UK32. Positions 21-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118144. 38 interactions.
IntActi Q9UK32. 28 interactions.
MINTi MINT-1424416.
STRINGi 9606.ENSP00000262752.

Chemistry

BindingDBi Q9UK32.
ChEMBLi CHEMBL4924.
GuidetoPHARMACOLOGYi 1530.

PTM databases

PhosphoSitei Q9UK32.

Polymorphism databases

DMDMi 11133131.

Proteomic databases

MaxQBi Q9UK32.
PaxDbi Q9UK32.
PRIDEi Q9UK32.

Protocols and materials databases

DNASUi 27330.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262752 ; ENSP00000262752 ; ENSG00000072133 . [Q9UK32-1 ]
ENST00000543399 ; ENSP00000440830 ; ENSG00000072133 . [Q9UK32-2 ]
ENST00000620340 ; ENSP00000483896 ; ENSG00000072133 . [Q9UK32-2 ]
GeneIDi 27330.
KEGGi hsa:27330.
UCSCi uc004eej.2. human. [Q9UK32-1 ]

Organism-specific databases

CTDi 27330.
GeneCardsi GC0XM083318.
HGNCi HGNC:10435. RPS6KA6.
HPAi HPA002852.
HPA003904.
MIMi 300303. gene.
neXtProti NX_Q9UK32.
PharmGKBi PA34850.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119016.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi Q9UK32.
KOi K04373.
OrthoDBi EOG7B8S38.
PhylomeDBi Q9UK32.
TreeFami TF313438.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_20510. RSK activation.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_22365. Recycling pathway of L1.
SignaLinki Q9UK32.

Miscellaneous databases

GenomeRNAii 27330.
NextBioi 35481255.
PROi Q9UK32.
SOURCEi Search...

Gene expression databases

Bgeei Q9UK32.
CleanExi HS_RPS6KA6.
ExpressionAtlasi Q9UK32. baseline and differential.
Genevestigatori Q9UK32.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016239. Ribosomal_S6_kinase_II.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 2 hits.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMARTi SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cerebellum.
  7. Cited for: FUNCTION IN P53/TP53 SIGNALING.
  8. "Functional characterization of human RSK4, a new 90-kDa ribosomal S6 kinase, reveals constitutive activation in most cell types."
    Duemmler B.A., Hauge C., Silber J., Yntema H.G., Kruse L.S., Kofoed B., Hemmings B.A., Alessi D.R., Froedin M.
    J. Biol. Chem. 280:13304-13314(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH MAPK3, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-232; SER-372; SER-389 AND THR-581, MUTAGENESIS OF SER-372; SER-389 AND THR-581.
  9. "The RSK family of kinases: emerging roles in cellular signalling."
    Anjum R., Blenis J.
    Nat. Rev. Mol. Cell Biol. 9:747-758(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-140; THR-258 AND ASN-692.

Entry informationi

Entry nameiKS6A6_HUMAN
AccessioniPrimary (citable) accession number: Q9UK32
Secondary accession number(s): B2R854
, B7ZL90, Q6FHX2, Q8WX28, Q9H4S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3